HEADER RNA BINDING PROTEIN 15-NOV-07 2ZD0
TITLE CRYSTAL STRUCTURES AND THERMOSTABILITY OF MUTANT TRAP3 A5 (ENGINEERED
TITLE 2 TRAP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION ATTENUATION PROTEIN MTRB;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: TRYPTOPHAN RNA-BINDING ATTENUATOR PROTEIN, TRP RNA-BINDING
COMPND 5 ATTENUATION PROTEIN, TRAP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1422;
SOURCE 4 STRAIN: NCA 26, ATCC 12980;
SOURCE 5 GENE: MTRB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS LINKER, ARTIFICIAL, ENGINEERED, RING PROTEIN, 12-MER, RNA BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WATANABE,Y.MISHIMA,I.YAMASHITA,S.Y.PARK,J.R.H.TAME,J.G.HEDDLE
REVDAT 4 01-NOV-23 2ZD0 1 REMARK SEQADV
REVDAT 3 08-FEB-17 2ZD0 1 TITLE VERSN
REVDAT 2 24-FEB-09 2ZD0 1 VERSN
REVDAT 1 29-APR-08 2ZD0 0
JRNL AUTH M.WATANABE,Y.MISHIMA,I.YAMASHITA,S.Y.PARK,J.R.TAME,
JRNL AUTH 2 J.G.HEDDLE
JRNL TITL INTERSUBUNIT LINKER LENGTH AS A MODIFIER OF PROTEIN
JRNL TITL 2 STABILITY: CRYSTAL STRUCTURES AND THERMOSTABILITY OF MUTANT
JRNL TITL 3 TRAP.
JRNL REF PROTEIN SCI. V. 17 518 2008
JRNL REFN ISSN 0961-8368
JRNL PMID 18287284
JRNL DOI 10.1110/PS.073059308
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 7503
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 363
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 511
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE SET COUNT : 22
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1519
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 39
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.35000
REMARK 3 B22 (A**2) : -0.35000
REMARK 3 B33 (A**2) : 0.71000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.609
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.301
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.185
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.967
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1591 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2141 ; 1.422 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 192 ; 7.103 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;31.180 ;23.108
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 283 ;16.015 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.298 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 245 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1181 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 529 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1015 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 83 ; 0.148 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 58 ; 0.184 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.129 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1007 ; 0.744 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1562 ; 1.235 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 664 ; 1.855 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 579 ; 3.034 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2ZD0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000027816.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 10.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7898
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.22100
REMARK 200 R SYM FOR SHELL (I) : 0.24600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 11.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2EXS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.09M CAPS PH 10.5, 30%(W/V) PEG300,
REMARK 280 0.15M AMMONIUM SULFATE, 10MM L-TRYPTOPHAN, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.83800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.83800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.83800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.83800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.83800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.83800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.83800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.83800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE POLYPEPTIDE CHAIN CONTAINS THREE (3) COPIES OF THE TRAP
REMARK 300 PROTEIN LINKED IN TANDEM, WHICH ARRANGE THEMSELVES TO MAKE A 12-MER
REMARK 300 RING IN SOLUTION. EACH CHAIN IN THIS MODEL REPRESENTS ONE COPY OF
REMARK 300 TRAP, NOT A SEPARATE POLYPEPTIDE. THE LINKER PEPTIDES ARE NOT
REMARK 300 VISIBLE IN THE ELECTRON DENSITY. THE 12MER RINGS ARE ALIGNED WITH
REMARK 300 THE CRYSTALLOGRAPHIC FOUR-FOLD AXIS. THERE ARE THREE COPIES OF TRAP
REMARK 300 PRESENT IN THE ASYMMETRIC UNIT. FOR THIS PROTEIN, CALLED T3A5, THE
REMARK 300 LINKER PEPTIDES CONSIST OF FIVE (5) ALANINE RESIDUES.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 109.67600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 54.83800
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -54.83800
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 54.83800
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 54.83800
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 3
REMARK 465 TYR A 4
REMARK 465 THR A 5
REMARK 465 ASN A 6
REMARK 465 ILE A 70
REMARK 465 GLU A 71
REMARK 465 SER A 72
REMARK 465 GLU A 73
REMARK 465 GLY A 74
REMARK 465 LYS A 75
REMARK 465 LYS A 76
REMARK 465 ALA A 77
REMARK 465 ALA A 78
REMARK 465 ALA A 79
REMARK 465 ALA A 80
REMARK 465 ALA A 81
REMARK 465 MET B 3
REMARK 465 TYR B 4
REMARK 465 THR B 5
REMARK 465 ASN B 6
REMARK 465 GLU B 73
REMARK 465 GLY B 74
REMARK 465 LYS B 75
REMARK 465 LYS B 76
REMARK 465 ALA B 77
REMARK 465 ALA B 78
REMARK 465 ALA B 79
REMARK 465 ALA B 80
REMARK 465 ALA B 81
REMARK 465 MET C 3
REMARK 465 TYR C 4
REMARK 465 THR C 5
REMARK 465 ASN C 6
REMARK 465 GLU C 73
REMARK 465 GLY C 74
REMARK 465 LYS C 75
REMARK 465 LYS C 76
REMARK 465 ALA C 77
REMARK 465 ALA C 78
REMARK 465 ALA C 79
REMARK 465 ALA C 80
REMARK 465 ALA C 81
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP A 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP B 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRP C 100
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EXS RELATED DB: PDB
REMARK 900 FUSION OF THREE TRAP MONOMERS
REMARK 900 RELATED ID: 2EXT RELATED DB: PDB
REMARK 900 FUSION OF FOUR TRAP MONOMERS
REMARK 900 RELATED ID: 1QAW RELATED DB: PDB
REMARK 900 B. STEAROTHERMOPHILUS WILD-TYPE TRAP
REMARK 900 RELATED ID: 2ZCZ RELATED DB: PDB
DBREF 2ZD0 A 3 76 UNP Q9X6J6 MTRB_BACST 1 74
DBREF 2ZD0 B 3 76 UNP Q9X6J6 MTRB_BACST 1 74
DBREF 2ZD0 C 3 76 UNP Q9X6J6 MTRB_BACST 1 74
SEQADV 2ZD0 ALA A 77 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA A 78 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA A 79 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA A 80 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA A 81 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA B 77 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA B 78 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA B 79 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA B 80 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA B 81 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA C 77 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA C 78 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA C 79 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA C 80 UNP Q9X6J6 LINKER
SEQADV 2ZD0 ALA C 81 UNP Q9X6J6 LINKER
SEQRES 1 A 79 MET TYR THR ASN SER ASP PHE VAL VAL ILE LYS ALA LEU
SEQRES 2 A 79 GLU ASP GLY VAL ASN VAL ILE GLY LEU THR ARG GLY ALA
SEQRES 3 A 79 ASP THR ARG PHE HIS HIS SER GLU LYS LEU ASP LYS GLY
SEQRES 4 A 79 GLU VAL LEU ILE ALA GLN PHE THR GLU HIS THR SER ALA
SEQRES 5 A 79 ILE LYS VAL ARG GLY LYS ALA TYR ILE GLN THR ARG HIS
SEQRES 6 A 79 GLY VAL ILE GLU SER GLU GLY LYS LYS ALA ALA ALA ALA
SEQRES 7 A 79 ALA
SEQRES 1 B 79 MET TYR THR ASN SER ASP PHE VAL VAL ILE LYS ALA LEU
SEQRES 2 B 79 GLU ASP GLY VAL ASN VAL ILE GLY LEU THR ARG GLY ALA
SEQRES 3 B 79 ASP THR ARG PHE HIS HIS SER GLU LYS LEU ASP LYS GLY
SEQRES 4 B 79 GLU VAL LEU ILE ALA GLN PHE THR GLU HIS THR SER ALA
SEQRES 5 B 79 ILE LYS VAL ARG GLY LYS ALA TYR ILE GLN THR ARG HIS
SEQRES 6 B 79 GLY VAL ILE GLU SER GLU GLY LYS LYS ALA ALA ALA ALA
SEQRES 7 B 79 ALA
SEQRES 1 C 79 MET TYR THR ASN SER ASP PHE VAL VAL ILE LYS ALA LEU
SEQRES 2 C 79 GLU ASP GLY VAL ASN VAL ILE GLY LEU THR ARG GLY ALA
SEQRES 3 C 79 ASP THR ARG PHE HIS HIS SER GLU LYS LEU ASP LYS GLY
SEQRES 4 C 79 GLU VAL LEU ILE ALA GLN PHE THR GLU HIS THR SER ALA
SEQRES 5 C 79 ILE LYS VAL ARG GLY LYS ALA TYR ILE GLN THR ARG HIS
SEQRES 6 C 79 GLY VAL ILE GLU SER GLU GLY LYS LYS ALA ALA ALA ALA
SEQRES 7 C 79 ALA
HET TRP A 100 15
HET TRP B 100 15
HET TRP C 100 15
HETNAM TRP TRYPTOPHAN
FORMUL 4 TRP 3(C11 H12 N2 O2)
FORMUL 7 HOH *39(H2 O)
SHEET 1 A 3 VAL A 43 GLN A 47 0
SHEET 2 A 3 PHE A 9 ALA A 14 -1 N VAL A 10 O ALA A 46
SHEET 3 A 3 ALA A 61 GLN A 64 -1 O GLN A 64 N VAL A 11
SHEET 1 B 7 PHE A 32 LEU A 38 0
SHEET 2 B 7 VAL A 19 THR A 25 -1 N VAL A 21 O GLU A 36
SHEET 3 B 7 THR A 52 ARG A 58 -1 O ALA A 54 N LEU A 24
SHEET 4 B 7 VAL B 43 GLN B 47 -1 O ILE B 45 N ILE A 55
SHEET 5 B 7 PHE B 9 ALA B 14 -1 N VAL B 10 O ALA B 46
SHEET 6 B 7 ALA B 61 THR B 65 -1 O TYR B 62 N LYS B 13
SHEET 7 B 7 GLY B 68 GLU B 71 -1 O GLY B 68 N THR B 65
SHEET 1 C 7 PHE B 32 LEU B 38 0
SHEET 2 C 7 VAL B 19 THR B 25 -1 N VAL B 21 O GLU B 36
SHEET 3 C 7 THR B 52 ARG B 58 -1 O LYS B 56 N ILE B 22
SHEET 4 C 7 VAL C 43 GLN C 47 -1 O GLN C 47 N SER B 53
SHEET 5 C 7 PHE C 9 ALA C 14 -1 N ILE C 12 O LEU C 44
SHEET 6 C 7 ALA C 61 THR C 65 -1 O TYR C 62 N LYS C 13
SHEET 7 C 7 GLY C 68 SER C 72 -1 O SER C 72 N ALA C 61
SHEET 1 D 3 PHE C 32 LEU C 38 0
SHEET 2 D 3 VAL C 19 THR C 25 -1 N VAL C 19 O LEU C 38
SHEET 3 D 3 THR C 52 ARG C 58 -1 O LYS C 56 N ILE C 22
SITE 1 AC1 12 THR A 25 ARG A 26 GLY A 27 ASP A 29
SITE 2 AC1 12 THR A 30 SER A 53 GLY B 23 GLN B 47
SITE 3 AC1 12 THR B 49 HIS B 51 THR B 52 HOH B 105
SITE 1 AC2 12 THR B 25 ARG B 26 GLY B 27 ASP B 29
SITE 2 AC2 12 THR B 30 SER B 53 GLY C 23 ALA C 46
SITE 3 AC2 12 GLN C 47 THR C 49 THR C 52 HOH C 101
SITE 1 AC3 11 GLY A 23 ALA A 46 GLN A 47 THR A 49
SITE 2 AC3 11 THR A 52 THR C 25 ARG C 26 GLY C 27
SITE 3 AC3 11 ASP C 29 THR C 30 SER C 53
CRYST1 109.676 109.676 36.756 90.00 90.00 90.00 P 4 21 2 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009118 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009118 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027206 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
